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The Mechanism of Catalysis of the Chorismate to Prephenate Reaction by the Escherichia coli Mutase Enzyme

Sun Hur and Thomas C. Bruice
Proceedings of the National Academy of Sciences of the United States of America
Vol. 99, No. 3 (Feb. 5, 2002), pp. 1176-1181
Stable URL: http://www.jstor.org/stable/3057734
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
The Mechanism of Catalysis of the Chorismate to Prephenate Reaction by the Escherichia coli Mutase Enzyme
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Abstract

Molecular dynamics studies of the Escherichia coli chorismate mutase (EcCM), containing at the active site chorismate and in turn the transition state (TS), have been performed. The simulations show that TS is not bound any tighter than chorismate. Comparison of average polar interactions show they are virtually identical for interactions of EcCM with chorismate and the TS, whereas hydrophobic interactions with TS are much weaker than with chorismate. Interactions and the mechanism of catalysis of chorismate → prephenate by the EcCM enzyme are discussed.

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